Treatment of human spermatozoa with seminal plasma inhibits protein tyrosine phosphorylation

被引:32
作者
Tomes, CN
Carballada, R
Moses, DF
Katz, DF
Saling, PM
机构
[1] Duke Univ, Med Ctr, Dept Obstet & Gynecol, Durham, NC 27710 USA
[2] Duke Univ, Med Ctr, Dept Cell Biol, Durham, NC 27710 USA
[3] Ctr Invest Reprod Perez Companc, RA-1084 Buenos Aires, DF, Argentina
[4] Duke Univ, Med Ctr, Dept Biomed Engn, Durham, NC 27710 USA
[5] Duke Univ, Med Ctr, Dept Obstet & Gynecol, Durham, NC 27710 USA
关键词
motility; phosphorylation; seminal plasma; spermatozoa; tyrosine;
D O I
10.1093/molehr/4.1.17
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
It has long been known that seminal plasma contains factors that influence the fertilizing capacity of spermatozoa in many different ways. However, little is understood of the biochemical cascades triggered when spermatozoa and seminal plasma interact. In this study, we examined how incubation with seminal plasma affected protein tyrosine phosphorylation in human spermatozoa. Increased protein tyrosine phosphorylation is a hallmark of sperm capacitation in several mammalian species, including human. Seminal plasma blocks protein tyrosine phosphorylation when added to washed, non-capacitated spermatozoa. Removal of seminar plasma and incubation in capacitating medium led to partial recovery of the tyrosine phosphorylation cascade. Addition of seminal plasma to a suspension of spermatozoa previously incubated for 5 h under capacitating conditions decreased the lever of tyrosine phosphorylation on all proteins in a dose-dependent manner. In this case, the phosphotyrosine signal did not increase upon removal of seminal plasma followed by overnight incubation in fresh capacitating media, indicating that removal of seminal plasma was necessary but not sufficient for protein tyrosine phosphorylation to occur. These results indicate that human seminal plasma contains factors that influence the tyrosine phosphorylation status of human spermatozoa.
引用
收藏
页码:17 / 25
页数:9
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